Applied Electrospray Mass Spectrometry: Practical by Birendra N. Pramanik, A.K. Ganguly, Michael L. Gross

By Birendra N. Pramanik, A.K. Ganguly, Michael L. Gross

Discussing techniques to figure out the constitution and machanisms of various compound classics, this publication covers new chemical and elctrophoretic strategies for speedy pattern preconcentration and separation. It summarizes breakthroughs within the idea and instrumentation of electrospray mass spectrometry in pharmaceutical and biomedical functions, presents functional examples for the characterization of peptides, proteins, and glycoproteins, comprises purposes in proteomics, combinatorial chemistry, and drug characterization. issues contain chemical and electrophoretic ideas for quick pattern preconcentration and separation, screening methods for proteins from libraries of compounds, protein folding and dynamics, and extra

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Additional info for Applied Electrospray Mass Spectrometry: Practical Spectroscopy Series Volume 32

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High speed separations can be accomplished by capillary electrophoresis or high speed liquid chromatography. For quantitative analysis, it is usually sufficient to monitor specific ions (selected ion monitoring) or reactions (selected reaction monitoring), and complete chromatographic separations are not always necessary. Excellent results were demonstrated by Romanyshyn et al. (287) by using high mobile-phase flow rates and short LC columns. Other applications may require data acquisition. Time-of-flight (TOF) mass spectrometry is well suited for high speed analysis, and an overview of TOF mass spectrometers will be presented in the discussion on mass analyzers for ESI-MS.

Proteins such as myoglobin or lysozyme produce a distribution of charge states (Fig. 8). The observed distribution of charges depends on both the solution-phase conditions and the ESI source conditions (302–314). The factors that affect charge-state distributions have been discussed in detail by Wang and Cole (302), and only a few examples will be mentioned here. Changing the protein conformation by changing the pH, solvent composition, or adding denaturants such as dithiothreitol (to reduce double bonds) can change the number of exposed basic sites, and this can affect the number of protons that can be attached (303).

Alkali metal cations such as sodium and potassium can be particularly troublesome for ESI-MS analysis of certain compound classes, especially oligonucleotides. Sulfate and phosphate impurities in protein samples can lead to adducts with a mass of 98 u; this can be eliminated by precipitating out the sulfate or phosphate prior to ESI-MS analysis (289). Common surfactants such as sodium dodecyl sulfate (SDS) or Triton X in protein samples can completely mask the presence of a protein signal. The use of a sample cleanup method such as microdialysis or of a separation method such as LC or CE can often eliminate or reduce the deleterious effect of impurities in a sample.

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